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PDP1  -  pyruvate dehyrogenase phosphatase...

Homo sapiens

 
 
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Disease relevance of PPM2C

  • After mutation of 9 ciliate Q codons (TAA) to CAA PtPP2C was expressed as an active protein in Escherichia coli [1].
  • The data imply that deficient activity of the PDH complex may be associated with spinocerebellar degenerations, and that the clinical phenotypes of the inherited ataxias can be associated with several genotypes [2].
  • The effects of diabetes on myocardial metabolism are complex in that they are tied to the systemic metabolic abnormalities of the disease (hyperglycemia and elevated levels of free fatty acid and ketone bodies), and changes in cardiomyocyte phenotype (e.g., down-regulation of glucose transporters and PDH activity) [3].
  • During the onset of exercise in hypoxia, the increased lactate accumulation is associated with a delayed activation of pyruvate dehydrogenase (PDH; Parolin ML, Spreit LL, Hultman E, Hollidge-Horvat MG, Jones NL, and Heigenhauser GJF. Am J Physiol Endocrinol Metab 278: E522-E534, 2000) [4].
  • We used an image analysis facility built around a PDP 11/105 computer to measure the volume of edema as outlined by Evans blue staining [5].
 

Psychiatry related information on PPM2C

  • PDP1 protein was not responsive to food deprivation in all fiber types [6].
  • Recent interest in PDP (parallel distributed processing) models is due in part to the widely held belief that they challenge many of the assumptions of classical cognitive science [7].
 

High impact information on PPM2C

  • A genomic clone encompassing the entire gene for the human pyruvate dehydrogenase beta subunit (PDH beta) has been isolated by screening a leukocyte genomic library with a nick-translated human foreskin fibroblast PDH beta cDNA probe [8].
  • The PDH beta structural gene is composed of 10 exons and 9 introns [8].
  • Primer-extension analysis indicated that the PDH beta gene transcription start site is an adenine residue located 132 bases upstream from the initiation codon in exon 1 [8].
  • The 5' flanking region of the PDH beta gene contains a "CAAT" consensus promoter sequence but no "TATA" sequence [8].
  • The amino acid sequences of phosphorylation sites determined in PDH alpha of bovine and porcine enzymes were also conserved in the human PDH alpha [9].
 

Chemical compound and disease context of PPM2C

 

Biological context of PPM2C

  • In intact cells, insulin exposure determined PDP1/2 phosphorylation, which was specifically prevented by PKCdelta antisense [12].
  • Decreased PDH activation and glycogenolysis during exercise following fat adaptation with carbohydrate restoration [13].
  • OBJECTIVE: The objective of this study was to determine whether down-regulation of pyruvate dehydrogenase phosphatase (PDP) is responsible for poorly active pyruvate dehydrogenase (PDH) in circulating lymphocytes (CLs) of obese subjects (ObS), and if so, whether it improves when their plasma insulin rises [14].
  • The catalytic subunit of PDP is a Mg2+-dependent enzyme homologous to the cytosolic phosphatases of the 2C family [15].
  • Thus, our results provide the first evidence that there are at least two isoenzymes of PDP in mammals that are different with respect to tissue distribution and kinetic parameters and, therefore, are likely to be different functionally [15].
 

Anatomical context of PPM2C

 

Associations of PPM2C with chemical compounds

  • During the oral glucose tolerance test, plasma insulin rose considerably more in ObS than in controls; PDHa and PDP1 activity also increased but remained significantly below normal, and PDHt was unvaried in both groups [14].
  • Instead, it is sensitive to the biological polyamine spermine, which, in turn, has no effect on the enzymatic activity of PDP1 [15].
  • Its activity toward the bovine 32P-labeled pyruvate dehydrogenase complex was Mg(2+)-dependent and Ca(2+)-stimulated and comparable to that of native bovine PDP [16].
  • Comparison of the deduced amino acid sequences of the mitochondrial PDPc and the rat cytosolic protein phosphatase 2C indicates that these protein serine/threonine phosphatases evolved from a common ancestor [16].
  • The amino acid sequences of NH2-terminal regions of the two subunits of human PDH were highly homologous with those of mature porcine PDH [9].
 

Physical interactions of PPM2C

  • Phosphatases that deactivate CFTR have yet to be identified definitively at the molecular level, however CFTR is regulated by a membrane-bound form of protein phosphatase-2C (PP2C) in several cell types [17].
 

Enzymatic interactions of PPM2C

 

Other interactions of PPM2C

 

Analytical, diagnostic and therapeutic context of PPM2C

References

  1. Functional characterization and localization of protein phosphatase type 2C from Paramecium. Grothe, K., Hanke, C., Momayezi, M., Kissmehl, R., Plattner, H., Schultz, J.E. J. Biol. Chem. (1998) [Pubmed]
  2. Pyruvate dehydrogenase deficiency in spinocerebellar degenerations. Kark, R.A., Rodriguez-Budelli, M. Neurology (1979) [Pubmed]
  3. Regulation of energy substrate metabolism in the diabetic heart. Stanley, W.C., Lopaschuk, G.D., McCormack, J.G. Cardiovasc. Res. (1997) [Pubmed]
  4. Effects of PDH activation by dichloroacetate in human skeletal muscle during exercise in hypoxia. Parolin, M.L., Spriet, L.L., Hultman, E., Matsos, M.P., Hollidge-Horvat, M.G., Jones, N.L., Heigenhauser, G.J. Am. J. Physiol. Endocrinol. Metab. (2000) [Pubmed]
  5. Enhancement of experimental cerebral edema after decompressive craniectomy: implications for the management of severe head injuries. Cooper, P.R., Hagler, H., Clark, W.K., Barnett, P. Neurosurgery (1979) [Pubmed]
  6. Skeletal muscle fiber type comparison of pyruvate dehydrogenase phosphatase activity and isoform expression in fed and food-deprived rats. Leblanc, P.J., Harris, R.A., Peters, S.J. Am. J. Physiol. Endocrinol. Metab. (2007) [Pubmed]
  7. Neural networks, nativism, and the plausibility of constructivism. Quartz, S.R. Cognition. (1993) [Pubmed]
  8. Molecular cloning and characterization of human pyruvate dehydrogenase beta subunit gene. Koike, K., Urata, Y., Koike, M. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  9. Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase. Koike, K., Ohta, S., Urata, Y., Kagawa, Y., Koike, M. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  10. Demonstration of type-R and type-C virus particles in hamster pancreatic adenocarcinomas. Sindelar, W.F., Tralka, T.S., Kurman, C.C., Hyatt, C.L., Henson, E.R. Cancer Lett. (1983) [Pubmed]
  11. Clinical experience and results of treatment with suprofen in pediatrics. 4th communication: Assessment of pain in babies and infants/Analgesic effect of suprofen syrup in otitis media. Weippl, G., Michos, N., Stocker, H. Arzneimittel-Forschung. (1985) [Pubmed]
  12. Activation and mitochondrial translocation of protein kinase Cdelta are necessary for insulin stimulation of pyruvate dehydrogenase complex activity in muscle and liver cells. Caruso, M., Maitan, M.A., Bifulco, G., Miele, C., Vigliotta, G., Oriente, F., Formisano, P., Beguinot, F. J. Biol. Chem. (2001) [Pubmed]
  13. Decreased PDH activation and glycogenolysis during exercise following fat adaptation with carbohydrate restoration. Stellingwerff, T., Spriet, L.L., Watt, M.J., Kimber, N.E., Hargreaves, M., Hawley, J.A., Burke, L.M. Am. J. Physiol. Endocrinol. Metab. (2006) [Pubmed]
  14. Down-regulation of pyruvate dehydrogenase phosphatase in obese subjects is a defect that signals insulin resistance. Piccinini, M., Mostert, M., Alberto, G., Ramondetti, C., Novi, R.F., Dalmasso, P., Rinaudo, M.T. Obes. Res. (2005) [Pubmed]
  15. Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino acid sequences, expression, and regulation. Huang, B., Gudi, R., Wu, P., Harris, R.A., Hamilton, J., Popov, K.M. J. Biol. Chem. (1998) [Pubmed]
  16. Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C. Lawson, J.E., Niu, X.D., Browning, K.S., Trong, H.L., Yan, J., Reed, L.J. Biochemistry (1993) [Pubmed]
  17. Regulation of the CFTR channel by phosphorylation. Dahan, D., Evagelidis, A., Hanrahan, J.W., Hinkson, D.A., Jia, Y., Luo, J., Zhu, T. Pflugers Arch. (2001) [Pubmed]
  18. Plasmodium protein phosphatase 2C dephosphorylates translation elongation factor 1beta and inhibits its PKC-mediated nucleotide exchange activity in vitro. Mamoun, C.B., Goldberg, D.E. Mol. Microbiol. (2001) [Pubmed]
  19. Cell cycle regulation and p53 activation by protein phosphatase 2C alpha. Ofek, P., Ben-Meir, D., Kariv-Inbal, Z., Oren, M., Lavi, S. J. Biol. Chem. (2003) [Pubmed]
  20. Molecular cloning and characterization of a novel human protein phosphatase 2C cDNA (PP2C epsilon*). Jin, F., Ji, C., Liu, L., Dai, J., Gu, S., Sun, X., Xie, Y., Mao, Y. Mol. Biol. Rep. (2004) [Pubmed]
  21. Regulation of the TAK1 signaling pathway by protein phosphatase 2C. Hanada, M., Ninomiya-Tsuji, J., Komaki , K., Ohnishi, M., Katsura, K., Kanamaru, R., Matsumoto, K., Tamura, S. J. Biol. Chem. (2001) [Pubmed]
  22. Regulation of recombinant cardiac cystic fibrosis transmembrane conductance regulator chloride channels by protein kinase C. Yamazaki, J., Britton, F., Collier, M.L., Horowitz, B., Hume, J.R. Biophys. J. (1999) [Pubmed]
  23. A lipoyl synthetic octadecapeptide of dihydrolipoamide acetyltransferase specifically recognized by anti-M2 autoantibodies in primary biliary cirrhosis. Tuaillon, N., Andre, C., Briand, J.P., Penner, E., Muller, S. J. Immunol. (1992) [Pubmed]
  24. A new protein phosphatase 2C (FsPP2C1) induced by abscisic acid is specifically expressed in dormant beechnut seeds. Lorenzo, O., Rodríguez, D., Nicolás, G., Rodríguez, P.L., Nicolás, C. Plant Physiol. (2001) [Pubmed]
  25. Antithrombin III: biodistribution in healthy volunteers. Knot, E.A., de Jong, E., ten Cate, J.W., Gie, L.K., van Royen, E.A. Thromb. Haemost. (1987) [Pubmed]
 
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